Comparative study on the rumen microbial populations, hydrolytic enzyme activities and dry matter degradability between different species of ruminant

Anim Sci J. 2010 Dec;81(6):642-7. doi: 10.1111/j.1740-0929.2010.00782.x. Epub 2010 Oct 7.

Abstract

A comparative study among Korean native cow (Hanwoo), Holstein dairy cow, Korean native goat and crossbred sheep on the population and marker concentration of ruminal microbes, the activities of carboxymethylcellulase (CMCase), xylanase and amylase, and in situ dry matter (DM) degradability were conducted. Twelve ruminally cannulated animals, three of each species, were used. Animals were fed the same diet containing 40% formula feed and 60% rice straw at the level of 2.5% of body weight. Total viable microbial populations in the rumen fluid were significantly (P < 0.01) greater for bacteria and fungi in goat than those of Holstein. The protozoan population among ruminant species was the reverse from that of bacteria. The concentrations of 2,6-diaminopimelic acid and chitin as markers for bacteria and fungi in the rumen fluid, respectively, were highest in goat, which is in accordance with the above population data. The concentration of aminoethylphosphonic acid as marker of protozoa was highest in Hanwoo and lowest in sheep (P < 0.01). Goat had the highest (P < 0.01) activities of all the enzymes investigated among ruminants. In situ effective degradation of the DM of rice straw was approximately 19% higher in the rumen of goat compared with other animals.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amylases / metabolism*
  • Animal Feed*
  • Animals
  • Bacteria / isolation & purification*
  • Cattle*
  • Cellulase / metabolism*
  • Ciliophora / isolation & purification*
  • Digestion*
  • Endo-1,4-beta Xylanases / metabolism*
  • Female
  • Fungi / isolation & purification*
  • Goats*
  • Rumen / enzymology*
  • Rumen / microbiology*
  • Rumen / parasitology
  • Sheep*
  • Species Specificity

Substances

  • Amylases
  • Cellulase
  • carboxymethylcellulase
  • Endo-1,4-beta Xylanases